Glycosidic bond specificity of glucansucrases: on the role of acceptor substrate binding residues

被引:50
作者
Leemhuis, Hans [1 ]
Pijning, Tjaard [1 ]
Dobruchowska, Justyna M. [1 ]
Dijkstra, Bauke W. [1 ]
Dijkhuizen, Lubbert [1 ]
机构
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst GBB, NL-9700 AB Groningen, Netherlands
关键词
alternansucrase; dextransucrase; glycoside hydrolase; reuteransucrase; lactic acid bacteria; protein engineering; AMINO-ACID-RESIDUES; ALPHA-AMYLASE FAMILY; LACTOBACILLUS-REUTERI STRAIN-180; CYCLODEXTRIN GLYCOSYLTRANSFERASE; DIRECTED EVOLUTION; STRUCTURAL-ANALYSIS; GTF-I; MOLECULAR CHARACTERIZATION; CHEMOENZYMATIC SYNTHESIS; FRUCTANSUCRASE ENZYMES;
D O I
10.3109/10242422.2012.676301
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Many lactic acid bacteria produce extracellular alpha-glucan polysaccharides using a glucansucrase and sucrose as glucose donor. The structure and the physicochemical properties of the alpha-glucans produced are determined by the nature of the glucansucrase. Typically, the alpha-glucans contain two types of alpha-glycosidic linkages, for example, (alpha 1-2), (alpha 1-3), (alpha 1-4) or (alpha 1-6), which may be randomly or regularly distributed. Usually, the alpha-glucan chains are also branched, which gives rise to an additional level of complexity. Even though the first crystal structure was reported in 2010, our current understanding of the structure-function relationships of glucansucrases is not advanced enough to predict the alpha-glucan specificity from the sequence alone. Nevertheless, based on sequence alignments and site-directed mutagenesis, a few amino acid residues have been identified as being important for the glycosidic bond specificity of glucansucrases. A new development in GH70 research was the identification of a cluster of alpha-glucan disproportionating enzymes. Here, we discuss the current insights into the structure-function relationships of GH70 enzymes in the light of the recently determined crystal structure of glucansucrases.
引用
收藏
页码:366 / 376
页数:11
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